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Genomics. 2000 Oct 1;69(1):143-9.

Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem.

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Department of Biochemistry, Saitama Medical School, Saitama, 350-0495, Japan.


We have cloned the full length of a novel cDNA, named ring finger protein 21 (RNF21), composed of the RING finger-B box-coiled coil (RBCC) domain and the B30.2 domain, which are characteristic of the RBCC-B30.2 family. As a structural feature, the RNF21 cDNA possessed at least three kinds of isoforms, due to alternative splicing, consisting of the long form with the RBCC-RBCC-B30.2 domain, the medium form with the RBCC-B30.2 domain, and the short form with only the RBCC domain. Moreover, respective transcripts corresponding to the three isoforms were detected in various human organs by reverse transcription-PCR and Northern blot analyses. Interestingly, the medium form of the RNF21 mRNA expressed most predominantly was dramatically up-regulated within 8-16 h by interferon stimulation of HeLa cells. These findings suggest that RNF21 is a downstream gene that may mediate interferon's biological action.

[Indexed for MEDLINE]

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